The Kinesin Superfamily Handbook

Abstract

In 2006, she joined the group of Jonathon Howard at the Max Planck Institute of Molecular Cell Biology and Genetics in Dresden, Germany. There, she solved the ATP turnover cycle of the microtubule depolymerising Kinesin-13, MCAK, and developed an interest in the kinesin superfamily of molecular motors. Since 2011, Claire has held the position of Assistant Professor at the University of Nottingham, UK. The research goals of the Friel lab are to understand the relationship between the kinesin motor domain sequence and the many functional properties of the kinesin superfamily and to understand the molecular mechanisms of proteins that regulate microtubule dynamics.

The legacy of kinesins in the pollen tube 30 years later

“…The “head” domain is responsible for the movement boosted by ATP hydrolysis while the “stalk/tail” domain is important for interacting with other subunits or cargo molecules such as proteins, lipids, or nucleic acids. A detailed description of the general structure of kinesins can be found in various reviews (Friel, 2020; Hirokawa & Takemura, 2004; Lawrence et al, 2004; Miki, Okada, & Hirokawa, 2005). Here, I propose only a summary of the various kinesin families.…”

Cytoskeletal diversification across 1 billion years: What red algae can teach us about the cytoskeleton, and vice versa

“…Abbreviations: Axo HCs, axonemally-associated dynein heavy chains (multiple types found in cilia and/or flagella); Cyt HC1, cytoplasmic dynein heavy chain 1; K1-15, numbered kinesin families; M1-11, numbered myosin families; MF, MyTH-FERM myosin (a group that contains MyTH-FERM domains and includes several numbered subgroups); P50, Arp1, components of the "Dynactin" complex (accessory to cytoplasmic dynein heavy chain 1). Adapted and updated from Figure 1 in Brawley et al, 2017 [10] moves towards the minus end of microtubules; also known as NCD) (Figure 2 and Table S3; Friel [45] provides reviews of the kinesin family).…”

“…While this is the full complement of kinesins in Porphyra umbilicalis, some red algae do have additional kinesins, specifically kinesin-4 (a kinesin that binds to chromatin, is involved in spindle assembly, and in some cell types also has trafficking roles), kinesin-6 (a kinesin that binds to the conserved spindle MT-crosslinker ASE1/PRC1 and is involved in cytokinesis), and kinesin-15 (a mitotic kinesin that appears to have functions overlapping those of kinesin-5). [45] This set of four kinesins means that Porphyra has one of the smallest complements of microtubule motors described thus far, and it provides insight into the minimal machinery needed to assemble a mitotic spindle. Consistent with a previous proposal based on work…”

“…[ 44 ] Even more striking is that the mitotic spindle of Porphyra assembles with only four classes of kinesin (Figure 2, Box 2, Table S3). Specifically, Porphyra has kinesin‐5 (a mitotic motor that is predicted to slide antiparallel microtubules; also known as BimC/Eg5), kinesin‐7 (a mitotic motor that typically localizes to centromeres and is thought to provide force for chromosome movement and/or spindle elongation; also known as CENP‐E), and kinesin‐14 (a mitotic motor with a C‐terminal motor that moves towards the minus end of microtubules; also known as NCD) (Figure 2 and Table S3; Friel [ 45 ] provides reviews of the kinesin family). In addition, Porphyra also has a pair of divergent kinesin family members that group weakly with kinesin‐13, a protein that functions as a microtubule depolymerase (also known as MCAK).…”

“…While this is the full complement of kinesins in Porphyra umbilicalis , some red algae do have additional kinesins, specifically kinesin‐4 (a kinesin that binds to chromatin, is involved in spindle assembly, and in some cell types also has trafficking roles), kinesin‐6 (a kinesin that binds to the conserved spindle MT‐crosslinker ASE1/PRC1 and is involved in cytokinesis), and kinesin‐15 (a mitotic kinesin that appears to have functions overlapping those of kinesin‐5). [ 45 ]…”